Zhilinskaya I N, Marchenko V A, Kharchenko E P
Research Institute of Influenza Named after A.A. Smorodintsev, Ministry of Health of Russian Federation, 197376 St. Petersburg, Russia.
North-Western State Medical University Named after I.I. Mechnikov, Ministry of Health of Russian Federation, 191015 St. Petersburg, Russia.
Mol Gen Microbiol Virol. 2022;37(4):209-225. doi: 10.3103/S0891416822040103. Epub 2023 Mar 20.
: To compare the repertoire of proteins of the human hemostatic system and fragments mimicking these proteins in the proteins of influenza A/H1N1 viruses and coronaviruses. . Influenza viruses A/H1N1 (A/Brevig Mission/1/18), A/St. Petersburg /RII04/2016 (H1N1)pdm09, coronaviruses SARS-CoV and SARS-CoV-2 (strain Wuhan-Hu-1) were used for comparative computer analysis. The sources of the primary structures of proteins of the analyzed viruses and 41 proteins of the human hemostatic system were publicly available Internet databases, respectively, www.ncbi.nlm.nih.gov and www.nextprot.org. The search for homologous sequences in the structure of viral proteins and hemostatic proteins was carried out by comparing fragments of 12 amino acids in length, taking as related those that showed identity at ≥8 positions. . Comparative analysis of the repertoire of cellular proteins of the hemostatic system and fragments mimicking these proteins in the structure of proteins of viruses A/H1N1 1918, A(H1N1)pdm09 isolated in 2016, SARS-CoV and SARS-CoV-2, showed a significant difference between SARS-CoV-2 and analyzed viruses. In the protein structure of the SARS-CoV-2 virus, mimicry was revealed for almost all analyzed hemostasis proteins. As for the comparison of viruses A/H1N1 1918, A(H1N1)pdm09 2016 and SARS-CoV, the influenza virus A/H1N1 1918 and SARS-CoV are the closest in the repertoire of hemostatic proteins. . Obtained bioinformatic analysis data can serve as a basis for further study of the role of homologous fragments in the regulation of hemostasis of the host organism.
比较人类止血系统的蛋白质库与甲型H1N1流感病毒和冠状病毒蛋白质中模拟这些蛋白质的片段。使用甲型H1N1流感病毒（A/布雷维格使命/1/18）、A/圣彼得堡/RII04/2016（H1N1）pdm09、冠状病毒SARS-CoV和SARS-CoV-2（武汉-胡-1株）进行比较计算机分析。所分析病毒的蛋白质一级结构来源和人类止血系统的41种蛋白质分别来自公开可用的互联网数据库，即www.ncbi.nlm.nih.gov和www.nextprot.org。通过比较长度为12个氨基酸的片段来搜索病毒蛋白和止血蛋白结构中的同源序列，将在≥8个位置显示相同性的片段视为相关片段。对止血系统的细胞蛋白库以及2016年分离的甲型H1N1流感病毒1918、A（H1N1）pdm09、SARS-CoV和SARS-CoV-2病毒结构中模拟这些蛋白的片段进行比较分析，结果显示SARS-CoV-2与所分析的病毒之间存在显著差异。在SARS-CoV-2病毒的蛋白质结构中，几乎所有分析的止血蛋白都存在模拟现象。至于甲型H1N1流感病毒1918、2016年的A（H1N1）pdm09和SARS-CoV的比较，甲型H1N1流感病毒1918和SARS-CoV在止血蛋白库方面最为接近。所获得的生物信息学分析数据可作为进一步研究同源片段在宿主生物体止血调节中作用的基础。
